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Related Experiment Videos

Complement inhibition by human vitronectin involves non-heparin binding domains

M Sheehan1, C A Morris, B A Pussell

  • 1Department of Nephrology, Prince Henry Hospital, Sydney, Australia.

Clinical and Experimental Immunology
|July 1, 1995
PubMed
Summary
This summary is machine-generated.

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Vitronectin inhibits complement-mediated cell lysis by blocking C5b-7 binding and C9 polymerization. Specific internal fragments, particularly a 43-kD region, were identified as crucial for these complement inhibition functions.

Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Vitronectin (complement S-protein) is a glycoprotein that inhibits complement-mediated cytolysis.
  • It acts at two stages of terminal complement complex (TCC) formation: C5b-7 binding and C9 polymerization.
  • The specific functional domains of vitronectin responsible for these inhibitory actions were not fully understood.

Purpose of the Study:

  • To identify the specific functional domains of vitronectin involved in inhibiting complement-mediated cytolysis.
  • To pinpoint the region responsible for blocking C5b-7 membrane binding.
  • To determine the site responsible for preventing C9 polymerization.

Main Methods:

  • Vitronectin was treated with cyanogen bromide (CNBr) to generate fragments of 12-kD, 53-kD, and 43-kD.

Related Experiment Videos

  • These fragments were tested for their ability to inhibit guinea pig erythrocyte (GPE) reactive lysis.
  • Assays were used to assess the binding of C5b-7 to immobilized vitronectin and C9 polymerization in the presence of C5b-8.

    • Main Results:

    • Native vitronectin, total CNBr digest, and the 53-kD and 43-kD fragments potently inhibited GPE reactive lysis.
    • The 43-kD fragment specifically blocked C5b-7 binding to immobilized vitronectin.
    • The 53-kD and 43-kD fragments prevented C5b-8-induced C9 polymerization, while the 12-kD fragment showed minimal inhibitory activity.

    Conclusions:

    • The C5b-7 binding site is localized to a 43-kD internal region of vitronectin.
    • Prevention of C5b-8-induced C9 polymerization is mediated by a site within an internal region of the vitronectin molecule.
    • These findings elucidate the specific domains of vitronectin responsible for its complement inhibitory functions.